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Reconstitution of catecholamine-stimulated adenylate cyclase activity using three purified proteins.
- Source :
-
The Journal of biological chemistry [J Biol Chem] 1985 Dec 15; Vol. 260 (29), pp. 15829-33. - Publication Year :
- 1985
-
Abstract
- beta-Adrenergic receptors, the GTP-binding regulatory protein that stimulates adenylate cyclase (Gs), and adenylate cyclase were each purified and reconstituted into unilamellar vesicles composed of phosphatidylethanolamine and phosphatidylserine (3:2, w/w). The molar ratio of receptor:Gs:adenylate cyclase was estimated to be about 1:10:1. Adenylate cyclase activity in the vesicles was stimulated up to 2.6-fold by beta-adrenergic agonists. Stimulation was dependent on the presence of guanine nucleotide, displayed appropriate beta-adrenergic selectivity and stereoselectivity for agonists, and was blocked appropriately by beta-adrenergic antagonists. Therefore, while additional proteins may modulate adenylate cyclase activity in native membranes, these results show that these three proteins are sufficient for the expression of hormone-stimulated adenylate cyclase.
- Subjects :
- Animals
Cattle
Cyclic AMP biosynthesis
Electrophoresis, Polyacrylamide Gel
Epinephrine pharmacology
Freeze Fracturing
In Vitro Techniques
Isoproterenol pharmacology
Lipid Bilayers metabolism
Microscopy, Electron
Propranolol pharmacology
Receptors, Adrenergic, beta metabolism
Stereoisomerism
Terbutaline pharmacology
Turkeys
Adenylyl Cyclases metabolism
Catecholamines pharmacology
GTP-Binding Proteins metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0021-9258
- Volume :
- 260
- Issue :
- 29
- Database :
- MEDLINE
- Journal :
- The Journal of biological chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 2999139